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PubMed2005

An in situ study of the t-butyllithium initiated polymerization of butadiene in d-heptane via small angle neutron scattering and 1H-NMR.

We present a combined 1H-NMR and small angle neutron scattering in situ study of the anionic polymerization of butadiene using t-butyllithium as the initiator. Both initiation and propagation phases were explored. This combined approach allows the structural and kinetic characteristics to be accessed and cross compared. The use of the D22 instrument (ILL Grenoble) permits the attainment of Q approximately equal to 2 x 10(-3) A. This, in turn, led to the identification of coexisting large-scale and smaller aggregates during all stages of the polymerization. The smaller aggregates contain most of the reacted monomers. Their structure changes from high functionality wormlike chains at early stages of the reaction to starlike aggregates where the crossover occurs at a degree of polymerization of approximately equal to 40. The initiation event involved these small, high functionality (approximately equal to 120) aggregates that apparently consisted of cross-associated t-butyllithium with the newly formed allylic-lithium head groups. As the initiation event progressed the initiation rate increased while the functionality of these small aggregates decreased and their size increased. Propagation, in the absence of initiation, was found to have a rate constant that was molecular weight dependent. At approximately 11 kg/mol the measured polymerization rate was found to increase while no further structural changes were seen.

Journal Article↗
PubMed2006

Dielectric relaxation and elasticity during polymerization.

A molecular kinetics-elasticity relation has been investigated by using real time dielectric spectroscopy of a diepoxide-triamine liquid mixture polymerizing at 298 K. As the liquid polymerized, the dielectric relaxation time tau increased linearly with the exponential of the known value of the instantaneous shear modulus G(infinity), in agreement with the elastic model for viscous flow but without the effect of temperature. Thus the structure-dependent effect on the Brownian motions are separated from the temperature-dependent effect. In this time-dependent process, increase in G(infinity) may be compensated by an increase in T, thereby keeping G(infinity) and tau constant. In the potential energy landscape paradigm, a polymerizing liquid's state point, like a normal liquid's on cooling, continuously shifts to deeper and lower energy minima of higher curvature, but the shift occurs irreversibly to other parts of the total energy landscape, thus adding a reaction coordinate to the landscape. A minimum in the energy landscape corresponding to a structure formed by polymerization may be identical to a minimum in another landscape corresponding to another structure.

Journal Article↗
PubMed2001

Fracture force, deflection at fracture, and toughness of repaired denture resin subjected to microwave polymerization or reinforced with wire or glass fiber.

STATEMENT OF PROBLEM: The ultimate goal of denture repair is to restore the denture's original strength and avoid further fracture. The best materials and methods for repair have not been conclusively determined. PURPOSE: This study investigated the fracture force, deflection at fracture, and toughness of a heat-polymerized denture base material repaired with heat-polymerized resin, autopolymerized resin alone, or autopolymerized resin with glass fiber or wire reinforcement. MATERIAL AND METHODS: Eight groups were evaluated: 6 with autopolymerized resin repairs, 1 with heat-polymerized resin repairs, and a control group of intact specimens. The 6 autopolymerized resin groups included 1 group with no reinforcement, 1 treated with microwave irradiation after polymerization, 2 with monolayer or multilayer glass fiber reinforcement, and 2 with round or braided wire reinforcement. Each group consisted of 12 specimens. The experimental specimens were cut, and a 3-mm butt joint gap was repaired as indicated by the group assignment. A 3-point bending test was used to determine the fracture force, deflection at fracture, and toughness of the specimens. The data were analyzed with 1-way analysis of variance and the Tukey post-hoc test (alpha=.05). RESULTS: The fracture force (28.4 to 73.4 N), deflection (1.6 to 3.8 mm), and toughness (0.02 to 0.13 J) values for all repaired groups were significantly lower than those for the control group (82.79 N, 4.4 mm, and 0.16 J, respectively), with one exception: the mean fracture force of specimens reinforced with round wire (102.9 N). Failure mode was always adhesive, meaning that fracture occurred between the denture base and repair resin. CONCLUSION: Among the repair treatments tested, the most effective was microwave-irradiated, autopolymerized resin reinforced with round wire or monolayer glass fiber ribbon.

Analysis of Variance↗
PubMed2002

Light-polymerized compomers: coefficient of thermal expansion and microhardness.

STATEMENT OF PROBLEM: The relationship between the filler content, coefficient of thermal expansion, and microhardness of commercial light-polymerized compomers has not been fully investigated. PURPOSE: This study evaluated the effect of filler content on the coefficient of thermal expansion and microhardness of 3 commercially available light-polymerized compomers. MATERIAL AND METHODS: Five specimens each from 3 commercially available compomers (Compoglass F, Elan and F2000) were evaluated. Linear thermal expansion (microm/ degrees C) was measured with a thermomechanical analyzer in the temperature range 20 degrees to 80 degrees C with increments of 10 degrees C. Standardized specimens were prepared in a metal die (1.5 x 2 x 12 mm) and polymerized for 40 seconds at 700 mW/cm(2) light intensity. The microhardness of 5 specimens from each of 3 compomers were measured with a Vickers hardness tester under a 15-second dwell time and 200-g load conditions. The specimens were polymerized at 700 mW/cm(2) intensity for 40 seconds after placing the compomers into a round aluminum mold. Differences in thermal expansion and microhardness among the compomers evaluated were statistically analyzed by use of one-way analysis of variance at P<.01 significance level, with differences assessed by use of Duncan's multiple range post hoc test. RESULTS: The coefficients of thermal expansion of Compoglass F (54.17 +/- 0.54 microm/ degrees C), Elan (40.94 +/- 0.78 microm/ degrees C) and F2000 (24.43 +/- 89 microm/ degrees C) were almost linear in the temperature range 25 degrees to 80 degrees C for all 3 compomers (r >.99). Inverse correlations between the %wt of filler and the coefficient of thermal expansion (r = -0.98, P<.0001), as well as between the microhardness and the coefficient of thermal expansion (r = -0.98, P<.0001) were observed. On the other hand, a linear correlation between the %wt of filler and microhardness of compomers was exhibited (r = -0.96, P<.0001). The microhardness values for Compoglass F, Elan, and F2000 were 43.82 +/- 1.62, 58.16 +/- 1.90, and 72.94 +/- 3.29, respectively. CONCLUSION: Within the limitations of this study, an inverse correlation between percent weight of filler and coefficient of thermal expansion, and a linear correlation between percent weight of filler and microhardness was observed for the evaluated compomers.

Analysis of Variance↗
PubMed2001

MMP9 production by human monocyte-derived macrophages is decreased on polymerized type I collagen.

The production of matrix metalloproteinases (MMPs), such as MMP9, by macrophages may be a critical factor in the rupture of unstable atherosclerotic plaques and aortic aneurysms. Therefore, we studied the role of matrix and soluble cytokines in the regulation of monocyte/macrophage expression of MMP9. Although freshly isolated monocytes synthesize little MMP9, cells cultured on tissue-culture plastic differentiate into macrophages and synthesize maximal amounts of MMP9. Differentiated macrophages cultured on plastic are unresponsive to further stimulation by interleukin 1beta, tumor necrosis factor alpha, or platelet-derived growth factor BB. In contrast, monocytes cultured on polymerized collagen synthesize much less MMP9 than cells cultured on plastic and demonstrate a more than three-fold increase in MMP9 synthesis in response to interleukin 1beta, tumor necrosis factor alpha, and platelet-derived growth factor BB. To determine whether the physical state of the collagen was critical for the decrease in basal synthesis of MMP9, monocytes were cultured in suspension for 5 days to allow differentiation and then seeded onto monomer or polymerized collagen. Synthesis of MMP9 was significantly decreased in cells on polymerized collagen and modestly increased in macrophages seeded on monomer collagen. These results suggest that MMP9 synthesis by macrophages in the vessel wall may be under negative control by native, polymerized collagen and that disruption of this native conformation could increase MMP9 production. In addition, cells in contact with the collagen matrix are potentially more responsive to soluble mediators such as platelet-derived growth factor, interleukin 1beta, and tumor necrosis factor alpha.

Aortic Aneurysm↗
PubMed2004

Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.

Actin, one of the most highly conserved and abundant eukaryotic proteins, is constantly being polymerized and depolymerized within cells as part of cellular motility, tissue formation and repair, and embryonic development. Many proteins exist that bind to monomeric or filamentous (F) forms of actin to regulate the polymerization state. It has become increasingly apparent that the ability of different proteins to bind to and regulate actin filament dynamics depends on the ability of the filament to exist in altered conformations. Yet, little is known about how these conformational changes occur at the molecular level. We have destabilized F-actin filaments by forming a disulfide that locks the "hydrophobic plug" to the body of the actin subunit or by altering the C terminus of actin with a tetramethylrhodamine label. We also examined F-actin filaments at short times after the initiation of polymerization. In all three cases, a substantial fraction of protomers can be found in a "tilted" state that also is induced by actin depolymerizing factor/cofilin proteins. These observations suggest that F-actin filaments are annealed over time into a stable filament and that actin-depolymerizing proteins can effect a time reversal of polymerization.

Actin Cytoskeleton↗
PubMed2006

Surface science of single-site heterogeneous olefin polymerization catalysts.

This article reviews the surface science of the heterogeneous olefin polymerization catalysts. The specific focus is on how to prepare and characterize stereochemically specific heterogeneous model catalysts for the Ziegler-Natta polymerization. Under clean, ultra-high vacuum conditions, low-energy electron irradiation during the chemical vapor deposition of model Ziegler-Natta catalysts can be used to create a "single-site" catalyst film with a surface structure that produces only isotactic polypropylene. The polymerization activities of the ultra-high vacuum-prepared model heterogeneous catalysts compare well with those of conventional Ziegler-Natta catalysts. X-ray photoelectron spectroscopic analyses identify the oxidation states of the Ti ions at the active sites. Temperature-programmed desorption distinguishes the binding strength of a probe molecule to the active sites that produce polypropylenes having different tacticities. These findings demonstrate that a surface science approach to the preparation and characterization of model heterogeneous catalysts can improve the catalyst design and provide fundamental understanding of the single-site olefin polymerization process.

Journal Article↗
PubMed2006

Study of ligand substituent effects on the rate and stereoselectivity of lactide polymerization using aluminum salen-type initiators.

A series of aluminum salen-type complexes [where salen is N,N'-bis(salicylaldimine)-1,2-ethylenediamine] bearing ligands that differ in their steric and electronic properties have been synthesized and investigated for the polymerization of rac-lactide. X-ray crystal structures on key precatalysts reveal metal coordination geometries intermediate between trigonal bipyramidal and square-based pyramidal. Both the phenoxy substituents and the backbone linker have a significant influence over the polymerization. Electron-withdrawing groups attached to the phenoxy donor generally gave an increased polymerization rate, whereas large ortho substituents generally slowed down the polymerization. The vast majority of the initiators afforded polylactide with an isotactic bias; only one exhibited a bias toward heteroselectivity. Isoselectivity generally increases with increased flexibility of the backbone linker, which is presumed to be better able to accommodate any potential steric clashes between the propagating polymer chain, the inserting monomer unit, and the substituents on the phenoxy donor.

Aluminum↗
PubMed2003

Probing polymerization forces by using actin-propelled lipid vesicles.

Actin polymerization provides a powerful propulsion force for numerous types of cell motility. Although tremendous progress has been made in identifying the biochemical components necessary for actin-based motility, the precise biophysical mechanisms of force generation remain unclear. To probe the polymerization forces quantitatively, we introduce an experimental system in which lipid vesicles coated with the Listeria monocytogenes virulence factor ActA are propelled by actin polymerization. The polymerization forces cause significant deformations of the vesicle. We have used these deformations to obtain a spatially resolved measure of the forces exerted on the membrane using a model based on the competition between osmotic pressure and membrane stretching. Our results indicate that actin exerts retractile or propulsive forces depending on the local membrane curvature and that the membrane is strongly bound to the actin gel. These results are consistent with the observed dynamics. After a slow elongation of the vesicle from a spherical shape, the strong bonds between the actin gel and the membrane rupture if the retractile forces exceed a critical value, leading to a rapid release of the vesicle's trailing edge.

Actins↗
PubMed1976

Reversible in vitro polymerization of tubulin from a cultured cell line (rat glial cell clone C6).

Tubulin from cultures of the rat glial cell clone C6 could be polymerized in vitro into intact microtubules. The polymerization was reversible and spontaneous, i.e., no addition of heterologous nucleation centers was necessary. Two cycles of polymerization/depolymerization yielded tubulin preparations of 95% purity as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electron microscopy was used to show that the microtubules assembled in vitro by two cycles of polymerization/depolymerization were morphologically intact and temperature sensitive. In contrast, tubulin from neuroblastoma cells, clone Neuro-2A, could not be polymerized in a reversible fashion. The discovery of a cell line from which tubulin can be reversibly polymerized in vitro establishes a model system for studies of cell-cycle- and cell-type-dependent regulatory mechanisms controlling the assembly of microtubules.

Cell Line↗
PubMed1977

Role of nucleotides in tubulin polymerization: effect of guanylyl 5'-methylenediphosphonate.

Incubation of 48,000 X g rat brain supernatants for 30 min at 37 degrees with 1-2 mM guanylyl 5'-methylenediphosphonate [Gmp(CH2)pp] results in polymerization of 95-98% of the tubulin present. This is considerably more than the 50% polymerization that can be achieved with the natural nucleotide, GTP, under optimal conditions. Gmp(CH2)pp is also much more effective than GTP in inducing polymerization of purified tubulin. Assembly of microtubules with Gmp(CH2)pp occurs at tubulin concentrations one-third of those possible with GTP. Furthermore, with Gmp(CH2)pp, microtubule assembly does not require the high molecular weight basic proteins needed with GTP. Polymerization of tubulin by Gmp(CH2)pp is neither prevented nor reversed by concentrations of calcium (2 mM) that can either prevent microtubule assembly or disrupt already formed microtubules if the nucleotide used is GTP or guanylyl imidodiphosphate. When Ca2+ is added before or after microtubule assembly, electron microscopy of the Gmp(CH2)pp preparations reveals normal microtubules turning into twisted ribbons. Low temperature (4 degrees) can both prevent and disrupt the tubulin assembled Gmp(CH2)pp although disruption proceeds much more slowly when GTP is used.

Animals↗
PubMed1977

Stoichiometry of GTP hydrolysis and tubulin polymerization.

Microtubule formation from lamb brain tubulin isolated by affinity chromatography and freed of exchangeable nucleotide requires GTP for maximal rate and extent of polymerization. The nucleotide analogs guanylylmethylenediphosphate and guanylylimidodiphosphate fail to replace GTP; in addition, neither the presence of microtubule associated proteins nor 5 M glycerol relieves the GTP requirement. The relation of GTP concentration and microtubule formation shows an association constant K = 1 X 10(4) M-1; furthermore, GDP and guanylylimidodiphosphate are competitive inhibitors of GTP for polymerization. Using a rapid filter assay for microtubule formation that allows the quantitative analysis of early polymerization kinetics and correcting for GTP hydrolysis uncoupled from tubulin polymerization, a stoichiometry of two molecules of GTP hydrolyzed per mole of tubulin dimer incorporated into microtubules has been found.

Animals↗
PubMed1985

Calmodulin accelerates the rate of polymerization of human platelet actin and alters the structural characteristics of actin filaments.

Calmodulin stimulated the rate of Mg2+-induced polymerization of human platelet actin. The stimulatory effect was due to an increase in the nucleation phase of the reaction; there was no effect on the steady-state viscosity. The calmodulin antagonist trifluoperazine blocked the stimulatory effect of calmodulin. Addition of EGTA to the reaction mixture also stimulated the rate of actin polymerization; however, the effect of calmodulin on actin polymerization is not due to Ca2+ chelation, as is presumed to be the case for EGTA. Electron microscopy revealed structural differences in the filaments prepared in the presence of calmodulin as compared to those prepared with trifluoperazine. In the presence of calmodulin, the filaments were thicker, suggesting that they consisted of multiple actin polymers. In addition, numerous projections were present perpendicular to the filaments, as well as localized areas of filament bundling. It was not possible to demonstrate a direct interaction between calmodulin and actin, which raises the possibility that the calmodulin effect may be indirect through a calmodulin-binding protein or calmodulin-dependent enzyme. Regardless of whether calmodulin is acting directly or indirectly, these results provide evidence that calmodulin may play a regulatory role in either the polymerization of actin or in determining the structural characteristics of actin filaments.

Actins↗
PubMed1990

Involvement of GTP-binding proteins in actin polymerization in human neutrophils.

The motility of human neutrophils, which is of vital importance for the role of these cells in host defense, is based on rapid and dynamic changes of the filamentous actin F-actin) network. Consequently, to understand how neutrophils move and ingest particles, we need to know how polymerization and depolymerization of actin are regulated. Previous studies by several investigators have, based on indirect evidence obtained with pertussis toxin, suggested a role for GTP-binding protein(s) (G protein) in chemotaxis-induced, but not phagocytosis-induced, reorganization of the F-actin network. The aim of the present investigation was to study the effects of directly activated G proteins (i.e., without prior ligand-receptor complex formation) on the F-actin content in human neutrophils. AlF4- induced a pronounced and sustained increase in F-actin in intact neutrophils. This effect coincided with an increase in cytosolic free Ca2+, indicating that phospholipase C and the subsequent transduction mechanism were also activated. Inhibition of phospholipase C activity by extensive depression of the cytosolic free Ca2+ level (less than 20 nM) only marginally affected the AlF4(-)-induced rise in F-actin content. The major part of the AlF4(-)-induced rise in F-actin content was also resistant to pertussis toxin, suggesting that pertussis toxin-insensitive G proteins in neutrophils are also able to trigger actin polymerization. The specificity of AlF4- in activating G proteins was also tested in permeabilized cells. In this case the effect was more rapid and could be totally abolished by guanosine 5'-[beta-thio]diphosphate. In analogy, in permeabilized cells guanosine 5'-[gamma-thio]triphosphate mimicked the effect of AlF4- on actin polymerization, and the effect induced by this nonhydrolyzable GTP analogue could also be totally abolished by guanosine 5'-[beta-thio]diphosphate. In summary, the present data support our previous hypothesis that G proteins are intimately linked to actin polymerization in human neutrophils.

Actins↗
PubMed1993

Polymerization of murine macrophage inflammatory protein 1 alpha inactivates its myelosuppressive effects in vitro: the active form is a monomer.

Macrophage inflammatory protein (MIP) 1 alpha has myelosuppressive and myeloprotective activity. That MIP-1 alpha polymerizes is known; this phenomenon was evaluated in terms of myelosuppression by assessing the effects of recombinant murine MIP-1 alpha on colony formation of murine and human myeloid progenitor cells in vitro. The following results are reported: (i) Polymerization is diluent- and concentration-dependent. (ii) Monomeric MIP-1 alpha is the active suppressive form for myeloid progenitor cells in vitro. (iii) Polymerized MIP-1 alpha is inactive and does not interfere with suppression by monomeric MIP-1 alpha. (iv) MIP-1 alpha has approximately 1000-fold higher specific activity than has been reported, but its effects are still specific for immature subsets of myeloid progenitors. (v) Suppression is initiated during the DNA-synthesis phase of the cell cycle. We conclude that polymerization of MIP-1 alpha might be a control mechanism that limits the myelosuppressive effects of monomeric MIP-1 alpha.

Animals↗
PubMed1994

GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules.

The FtsZ protein is a GTPase that is essential for cell division in Escherichia coli. During cytokinesis, FtsZ localizes to a ring at the leading edge of septum synthesis. We report the GTP-dependent polymerization of purified FtsZ measured by sedimentation and light scattering. Electron microscopy of polymerized FtsZ revealed structures including tubules 14-20 nm in diameter with longitudinal arrays of protofilaments. FtsZ depolymerized upon removal of GTP and repolymerized after subsequent GTP addition. Mutant FtsZ84 protein polymerized inefficiently, suggesting that polymerization is important for the cellular role of FtsZ in division. The possibility that tubules of FtsZ protein form a cytoskeleton involved in septum synthesis is consistent with our data.

Bacterial Proteins↗
PubMed1995

Roles of heavy and light chains in IgM polymerization.

IgM antibodies are secreted as multisubunit polymers that consist of as many as three discrete polypeptides: mu heavy chains, light (L) chains, and joining (J) chains. We wished to determine whether L chains that are required to confer secretory competence on immunoglobulin molecules must be present for IgM to polymerize--that is, for intersubunit disulfide bonds to form between mu chains. Using a L-chain-loss variant of an IgM-secreting hybridoma, we demonstrated that mu chains were efficiently polymerized independent of L chains, in a manner similar to that observed for conventional microL complexes, and that the mu polymers incorporated J chain. These mu polymers were not secreted but remained associated with the endoplasmic reticulum-resident chaperone BiP (GRP78). This finding is consistent with the endoplasmic reticulum being the subcellular site of IgM polymerization. We conclude that mu chain alone has the potential to direct the polymerization of secreted IgM, a process necessary but not sufficient for IgM to attain secretory competence.

Animals↗
PubMed1997

The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.

After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the alpha chain of one fibrin molecule and the C-terminal region of a gamma chain of an adjacent fibrin(ogen) molecule. In this report, the polymerization pocket has been identified by determining the crystal structure of a 30-kDa C-terminal fragment of the fibrin(ogen) gamma chain complexed with the peptide Gly-Pro-Arg-Pro. This peptide mimics the N terminus of the alpha chain of fibrin. The conformational change in the protein upon binding the peptide is subtle, with electrostatic interactions primarily mediating the association. This is consistent with biophysical experiments carried out over the last 50 years on this fundamental polymerization reaction.

Dimerization↗